PA2TI_NAJHH
ID PA2TI_NAJHH Reviewed; 48 AA.
AC P0DUG4;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=phospholipase A2 TI-Nh {ECO:0000303|PubMed:19622365};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:19622365};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Thrombin inhibitor from Naja haje {ECO:0000303|PubMed:19622365};
DE Flags: Fragments;
OS Naja haje haje (Egyptian cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8642;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19622365; DOI=10.1016/j.toxicon.2009.07.011;
RA Osipov A.V., Filkin S.Y., Makarova Y.V., Tsetlin V.I., Utkin Y.N.;
RT "A new type of thrombin inhibitor, noncytotoxic phospholipase A2, from the
RT Naja haje cobra venom.";
RL Toxicon 55:186-194(2010).
CC -!- FUNCTION: Phospholipase A2 with weak enzymatic activity, which inhibits
CC partially inhibits thrombin enzymatic activity (Ki=73 nM), completely
CC inhibits thrombin-induced platelet aggregation and retards fibrin clot
CC formation (IC(50)=0.2 nM) (PubMed:19622365). May exert this
CC anticoagulant effect through a non-enzymatic mechanism
CC (PubMed:19622365). Does not exert detectable effects on both the
CC intrinsic and extrinsic pathways of the coagulation cascade (up to 50
CC nM) (PubMed:19622365). Does not hydrolyze either fibrinogen or thrombin
CC (PubMed:19622365). Does not have impact on already formed fibrin clot
CC (PubMed:19622365). Is not toxic to PC12 tumor cells (up to 15 uM), but
CC evokes neurite outgrowth in these cells (1 uM) (PubMed:19622365). Has
CC not effect on ADP-induced platelet aggregation (PubMed:19622365).
CC {ECO:0000269|PubMed:19622365}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC ProRule:PRU10036, ECO:0000269|PubMed:19622365};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=0.0012 umol/min/mg enzyme (from PMID:25522251);
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19622365}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19622365}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:19622365}.
CC -!- MASS SPECTROMETRY: Mass=14340; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19622365};
CC -!- MISCELLANEOUS: The active site (His-25) is not easily accessible for
CC modification by 4-bromophenacyl bromide (BPB).
CC {ECO:0000269|PubMed:19622365}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0DUG4; -.
DR SMR; P0DUG4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR SUPFAM; SSF48619; SSF48619; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade inhibiting toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Platelet aggregation inhibiting toxin; Secreted;
KW Toxin.
FT CHAIN 1..48
FT /note="phospholipase A2 TI-Nh"
FT /evidence="ECO:0000269|PubMed:19622365"
FT /id="PRO_0000452214"
FT ACT_SITE 25
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 11..?
FT /evidence="ECO:0000305"
FT DISULFID 21..?
FT /evidence="ECO:0000305"
FT DISULFID 22..?
FT /evidence="ECO:0000305"
FT DISULFID 28..?
FT /evidence="ECO:0000305"
FT DISULFID 38..?
FT /evidence="ECO:0000305"
FT NON_CONS 20..21
FT /evidence="ECO:0000305"
FT NON_TER 48
FT /evidence="ECO:0000305"
SQ SEQUENCE 48 AA; 5481 MW; 9DD392852315A403 CRC64;
NVYQYRKMLQ CAMPNGGPFE CCQTHDNCYG EAEKLKACTS THSSPYFK
